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Xenopus oocyte maturation requires the phosphorylation and activation of p42 mitogen-activated protein kinase (MAPK). Likewise, the dephosphorylation and inactivation of p42MAPK are critical for the progression of fertilized eggs out of meiosis and through the first mitotic cell cycle. Whereas the kinase responsible for p42MAPK activation is well characterized, little is known concerning the phosphatases that inactivate p42MAPK. We designed a microinjection-based assay to examine the mechanism of p42MAPK dephosphorylation in intact oocytes. We found that p42MAPK inactivation is mediated by at least two distinct phosphatases, an unidentified tyrosine phosphatase and a protein phosphatase 2A-like threonine phosphatase. The rates of tyrosine and threonine dephosphorylation were high and remained constant throughout meiosis, indicating that the dramatic changes in p42MAPK activity seen during meiosis are primarily attributable to changes in MAPK kinase activity. The overall control of p42MAPK dephosphorylation was shared among four partially rate-determining dephosphorylation reactions, with the initial tyrosine dephosphorylation of p42MAPK being the most critical of the four. Our findings provide biochemical and kinetic insight into the physiological mechanism of p42MAPK inactivation.
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